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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Eukaryotic translation initiation factor 4A3

This gene encodes a member of the DEAD box protein family. DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. The protein encoded by this gene is a nuclear matrix protein. Its amino acid sequence is highly similar to the amino acid sequences of the translation initiation factors eIF4AI and eIF4AII, two other members of the DEAD box protein family. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Y14, caspase-3, MLN51, Magoh, ATPase
Papers on eIF4AIII
The eIF4AIII RNA helicase is a critical determinant of human cytomegalovirus replication.
Moorman et al., Chapel Hill, United States. In Virology, Feb 2016
We found that the eIF4AIII RNA helicase, a component of the exon junction complex, was necessary for efficient virus replication.
Coordinated function of cellular DEAD-box helicases in suppression of viral RNA recombination and maintenance of viral genome integrity.
Nagy et al., Lexington, United States. In Plos Pathog, Feb 2015
Interestingly, another co-opted cellular helicase, the eIF4AIII-like AtRH2, enhances TBSV recombination in the absence of Ded1/RH20, suggesting that the coordinated actions of these helicases control viral RNA recombination events.
CLIP-seq to discover transcriptome-wide imprinting of RNA binding proteins in living cells.
Le Hir et al., Paris, France. In Methods Mol Biol, 2014
Here, we describe in detail the protocol we employed to identify RNA targets of the human RNA helicase eIF4AIII.
eIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5'UTR.
Kim et al., Seoul, South Korea. In Proc Natl Acad Sci U S A, 2014
Here, we demonstrate the previously unappreciated role of eukaryotic translation initiation factor 4AIII (eIF4AIII), a component of EJC, in the translation of mRNAs bound by the nuclear cap-binding complex (CBC), a heterodimer of cap-binding protein 80 (CBP80) and CBP20.
Long Noncoding RNAs in Interaction With RNA Binding Proteins in Hepatocellular Carcinoma.
Mohamadkhani, Tehrān, Iran. In Hepat Mon, 2014
Besides, this study predicted that eIF4AIII, PTB and FUS were the most involved RBPs in interaction with HCC-related lncRNAs.
The expanding functions of cellular helicases: the tombusvirus RNA replication enhancer co-opts the plant eIF4AIII-like AtRH2 and the DDX5-like AtRH5 DEAD-box RNA helicases to promote viral asymmetric RNA replication.
Nagy et al., Lexington, United States. In Plos Pathog, 2014
In this paper, we have discovered a second group of cellular RNA helicases, including the eIF4AIII-like yeast Fal1p and the DDX5-like Dbp3p and the orthologous plant AtRH2 and AtRH5 DEAD box helicases, which are co-opted by tombusviruses.
A noncoding expansion in EIF4A3 causes Richieri-Costa-Pereira syndrome, a craniofacial disorder associated with limb defects.
Passos-Bueno et al., Bauru, Brazil. In Am J Hum Genet, 2014
Sequencing strategies identified an expansion of a region with several repeats of 18- or 20-nucleotide motifs in the 5' untranslated region (5' UTR) of EIF4A3, which contained from 14 to 16 repeats in the affected individuals and from 3 to 12 repeats in 520 healthy individuals.
Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box protein is inhibited by a MIF4G domain.
Conti et al., München, Germany. In Proc Natl Acad Sci U S A, 2013
We determined the 2.0-Å resolution structure of the complex of human eIF4AIII and the MIF4G domain of the splicing factor Complexed With Cef1 (CWC22), an essential prerequisite for exon junction complex assembly by the splicing machinery.
Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex.
Steitz et al., New Haven, United States. In Genes Dev, 2011
demonstrate direct physical interactions between yeast Sgd1p and Fal1p, and between their human orthologs (NOM1 and eIF4AIII) in vitro and in vivo, identifying human NOM1 as a missing eIF4G-like interacting partner of eIF4AIII
Exon junction complex subunits are required to splice Drosophila MAP kinase, a large heterochromatic gene.
Treisman et al., United States. In Cell, 2010
MAPK expression also requires the EJC subunits Y14 and eIF4AIII and EJC-associated splicing factors.
Structural aspects of RNA helicases in eukaryotic mRNA decay.
Song et al., Singapore, Singapore. In Biosci Rep, 2009
In the present review, we focus on the structural and mechanistic aspects of three RNA helicases, Dhh1, Upf1 and eIF4AIII, that are involved in eukaryotic mRNA decay.
The NMD mRNA surveillance pathway downregulates aberrant E-cadherin transcripts in gastric cancer cells and in CDH1 mutation carriers.
Oliveira et al., Porto, Portugal. In Oncogene, 2008
The nonsense-mediated-decay mRNA surveillance pathway downregulates aberrant E-cadherin transcripts in gastric cancer cells and in CDH1 mutation carriers.
Structural insights into the exon junction complex.
Andersen et al., Gif-sur-Yvette, France. In Curr Opin Struct Biol, 2008
In the complex, mRNA binding is mediated by the DEAD-box protein eIF4AIII, and inhibition of its ATPase activity forms the mechanistic basis for the long-term stability of the complex.
The EJC factor eIF4AIII modulates synaptic strength and neuronal protein expression.
Moore et al., Waltham, United States. In Cell, 2007
Data show that eIF4AIII, a core exon junction complex (EJC) component loaded onto mRNAs by pre-mRNA splicing, is associated with neuronal mRNA granules and dendritic mRNAs.
Splicing remodels messenger ribonucleoprotein architecture via eIF4A3-dependent and -independent recruitment of exon junction complex components.
Krainer et al., United States. In Proc Natl Acad Sci U S A, 2007
Although it is dispensable for pre-mRNA splicing in vitro, eIF4A3 is required for splicing-dependent loading of the Y14-Magoh core heterodimer onto mRNA.
Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.
Andersen et al., Århus, Denmark. In Science, 2006
crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase eukaryotic initiation factor 4AIII bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic
The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA.
Conti et al., Heidelberg, Germany. In Cell, 2006
The complex is formed by the association of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP.
An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay.
Izaurralde et al., Cambridge, United Kingdom. In Nature, 2004
identification of eIF4AIII and Barentsz as components of a conserved protein complex that is essential for mRNA localization in flies and nonsense-mediated mRNA decay in mammals
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